ID I0TCS0_9BACT Unreviewed; 263 AA.
AC I0TCS0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Acid phosphatase {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000897};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000897};
GN Name=pho_2 {ECO:0000313|EMBL:EID33423.1};
GN ORFNames=HMPREF9969_1834 {ECO:0000313|EMBL:EID33423.1};
OS Prevotella sp. oral taxon 306 str. F0472.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID33423.1, ECO:0000313|Proteomes:UP000004421};
RN [1] {ECO:0000313|EMBL:EID33423.1, ECO:0000313|Proteomes:UP000004421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0472 {ECO:0000313|EMBL:EID33423.1,
RC ECO:0000313|Proteomes:UP000004421};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000032,
CC ECO:0000256|PIRNR:PIRNR000897};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009017, ECO:0000256|PIRNR:PIRNR000897}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EID33423.1}.
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DR EMBL; AJIN01000040; EID33423.1; -; Genomic_DNA.
DR RefSeq; WP_009435053.1; NZ_AJIN01000040.1.
DR AlphaFoldDB; I0TCS0; -.
DR STRING; 1095752.HMPREF9969_1834; -.
DR PATRIC; fig|1095752.3.peg.1308; -.
DR eggNOG; COG0671; Bacteria.
DR OrthoDB; 9805301at2; -.
DR Proteomes; UP000004421; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd03397; PAP2_acid_phosphatase; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR001011; Acid_Pase_classA_bac.
DR InterPro; IPR018296; Acid_Pase_classA_bac_CS.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000897; Acid_Ptase_ClsA; 1.
DR PRINTS; PR00483; BACPHPHTASE.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR PROSITE; PS01157; ACID_PHOSPH_CL_A; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000897, ECO:0000313|EMBL:EID33423.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..263
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003634986"
FT DOMAIN 117..229
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 263 AA; 28996 MW; A0B74CCEE7940308 CRC64;
MTKKALIVGF VAMLSLSTFA QTASTKIKDA RTKPDLYFLQ DGQQASSLDL LPPPPQLGSI
QFLYDEAQYQ WGKMQRDTPR GDQAAADARV GGDGVPNAFS EAFGVKISKE TTPEIYKLIL
NMREDAGDLA TRGAKDHYMR VRPFAFYKEM TCNPEQQQEL STNGSYPSGH TAIGWATALV
LAEINVDRQN EILERGYQMG QSRVICGYHW QSDVDAARII SAAIVARLHA DPAFQAQLAK
AKKEFAKLQK DGKVAKSTFK AAN
//
